Summary
Phage lysozyme
This family includes lambda phage lysozyme and E. coli endolysin.
Literature references
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Weaver LH, Matthews BW; , J Mol Biol 1987;193:189-199.: Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. PUBMED:3586019
InterPro entry IPR002196
O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families PUBMED:7624375, PUBMED:8535779, PUBMED:. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site PUBMED:. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Glycoside hydrolase family 24 comprises enzymes with only one known activity; lysozyme ().
This entry includes Bacteriophage lambda lysozyme and Escherichia coli endolysin PUBMED:3586019. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryotic cell walls. E. coli endolysin also functions in bacterial cell lysis and acts as a transglycosylase. The Bacteriophage T4 lysozyme structure contains 2 domains, the interface between which forms the active-site cleft. The N-terminus of the 2 domains undergoes a 'hinge-bending' motion about an axis passing through the molecular waist PUBMED:3586019, PUBMED:2234094. This mobility is thought to be important in allowing access of substrates to the enzyme active site.
Clan
This family is a member of clan Lysozyme (CL0037), which contains the following 10 members:
DUF847 Glucosaminidase Glyco_hydro_19 Glyco_hydro_46 Lys Phage_lysozyme REGB_T4 SLT TraH_2 TransglycosylasGene Ontology
| Molecular function | lysozyme activity (GO:0003796) |
| Biological process | cell wall macromolecule catabolic process (GO:0016998) |
| peptidoglycan catabolic process (GO:0009253) |
External database links
| CAZY: | GH_24 |
| PANDIT: | PF00959 |
| SCOP: | 119l |
| SYSTERS: | Phage_lysozyme |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Sarah Teichmann |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A, Griffiths-Jones SR |
| Number in seed: | 18 |
| Number in full: | 951 |
| Average length of the domain: | 111.50 aa |
| Average identity of full alignment: | 25 % |
| Average coverage of the sequence by the domain: | 57.12 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 110 | ||||||||||||
| Family (HMM) version: | 12 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Phage_lysozyme domain has been found.
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